Purification and characterization of the proline-rich proteins from rabbit parotid saliva by Andrew I. Spielman Download PDF EPUB FB2
One of the families of inhibitory proteins in human and monkey saliva is the acidic proline-rich proteins. The purpose of this study was to isolate and characterize inhibitors of calcium phosphate precipitation from rabbit parotid saliva. Saliva was fractionated by immunoaffinity chromatography and anion exchange by: 9.
Spielman A. and Benniek A. () Isolation and character- ization of six proteins from rabbit parotid saliva belonging to a unique family of proline-rich proteins.
Archs oral Biol. 34, Wong R. and Benniek A. () The primary structure of a salivary calcium-binding proline-rich phosphoprotein (protein C), a possible precursor of a Cited by: 9. Rabbit parotid saliva was collected and proline-rich proteins were affinity purified using goat antibodies to human proline-rich proteins.
Further purification was achieved by repeated cation exchange chromatography on a Mono S column using a Fast Protein Liquid Chromatography by: Purification and characterization of a rabbit salivary protein, a potent inhibitor of crystal growth of calcium phosphate salts.
Isolation and characterization of six proteins from rabbit parotid saliva belonging to a unique family of proline-rich proteins. Archives of Oral Biology34 (2), Cited by: The obser- vation that rabbit saliva fails to react with antiserum to human proline-rich protein A, but shows partial cross-reactivity with the antiserum to human protein C, suggests that the rabbit proteins are more similar to the C-terminal part of human protein C, which is not found in human protein A, than the N-terminal part which is common to human proteins A and C (Wong and Bennick, ).Cited by: title = "Purification and characterization of a rabbit salivary protein, a potent inhibitor of crystal growth of calcium phosphate salts", abstract = "Human saliva is supersaturated with respect to basic calcium phosphate salts but is stabilized by specific macromolecules that inhibit calcium phosphate by: 9.
Purification and characterization of a glycosylated proline-rich protein from human parotid saliva. International Journal of Biochemistry24 (7), DOI: /X(92) by: Salivary proline-rich proteins and glycoproteins have been reported to show two abnormal character- istics on SDS-PAGE: (i) the proline-rich proteins stain pink-violet with Coomassie brilliant blue, and (ii) because of high carbohydrate content, the mol- ecular weight of the glycoprotein, as indicated by the migration distance into the gel, does not agree with the molecular weight as determined by Cited by: Purification and characterization of proline-rich proteins from developing embryos of the camel tick Hyalomma dromedarii Article (PDF Available) in Comparative biochemistry and physiology.
Proline-rich proteins from human parotid saliva. Isolation and partial characterization. Parotid saliva contains a variety of proline‐rich proteins. This study found that, among children between the ages of 5 to 15 years, there is a significant increase in the decayed‐missing‐filled tooth surface (DMFS) score of the permanent teeth with age in children with the specific proline‐rich protein phenotypes Pa and by: Four proteins, which have been designated A, B, C and D, have been purified from human parotid saliva.
These proteins are the major constituents of parotid saliva which migrate rapidly to the anode in polyacrylamide electrophoresis at pH Gel filtration and polyacrylamide electrophoresis were employed in the purification by: Differential expression of proline-rich proteins in rabbit salivary glands Article (PDF Available) in Journal of Histochemistry and Cytochemistry 40(9) October with 56 Reads.
Rabbit parotid saliva was collected and proline-rich proteins were affinity purified using goat antibodies to human proline-rich proteins. Purification was achieved by repeated cation exchange.
The estimated secretions of proline-rich proteins, when calculated on the basis of the three respective amino acids, wereand mg of proline-rich proteins per 10 mg of additional hull.
Basic proline-rich proteins constitute a smaller percentage of the total protein in rat parotid saliva than they do in human parotid saliva ( versus 40 per cent).
Purification and Characterization of a Proline‐Rich Antibacterial Peptide, with Sequence Similarity to Bactenecin‐7, from the Haemocytes of the Shore Crab, Carcinus Maenas Denni Schnapp Gatty Marine Laboratory, School of Biological and Medical Sciences, University of St Andrews, ScotlandCited by: Bennick A, Connell GE.
Purification and partial characterization of four proteins from human parotid saliva. Biochem J. Jul; (3)– Blaschko H, Firemark H, Smith AD, Winkler H. Lipids of the adrenal medulla. Lysolecithin, a characteristic constituent of chromaffin granules.
Biochem J. Aug; (2)– Abstract. Human saliva contains a large number of phosphopeptides derived by cleavage of acidic proline-rich proteins (APRPs). These peptides were purified by column chromatography and they constituted % of APRPs in parotid saliva, but 11% of APRPs in saliva expectorated from the mouth (whole saliva), indicating that there is considerable cleavage of APRPs after secretion from the Cited by: Spielman, A.I.
(): Purification and Characterization of the Proline-rich Proteins from Rabbit Parotid Saliva, Ph.D. Thesis, Univ.
of Toronto, Toronto. Google Scholar Spielman, A.I. and Bennick, A. (): Isolation and Characterization of Six Proteins from Rabbit Parotid Saliva Belonging to a Unique Family of Proline-rich Proteins, Arch Cited by: The role of human salivary acidic proline-rich proteins in the formation of acquired dental pellicle in vivo and their fate after adsorption to the human enamel surface.
Arch Oral Biol. ; 28 (1)– Bennick A, Connell GE. Purification and partial characterization of four proteins from human parotid by: Presentation of techniques for purifying proteins, with some information on Mass Spec and Crystallography, Protein, purification, biochemistry, David A. John.
The salivary glands of animals have great potential to act as powerful bioreactors to produce human therapeutic proteins. Human nerve growth factor (hNGF) is an important pharmaceutical protein Cited by: 1. Basic salivary proline-rich protein 2 Add BLAST: Chain i PRO_ 17 – Basic proline-rich peptide IB-1 Add BLAST: Chain i PRO_ 52 – Basic proline-rich peptide P-E Add BLAST: Chain i PRO_ – Basic proline-rich peptide IB-7 Add BLAST: Chain i PRO_ – Basic.
An enzyme was purified from human parotid saliva that can cleave a single arginine-glycine peptide bond between residues and in human salivary proline-rich protein C, hereby giving rise to another proline-rich protein A, which is also found in saliva Cited by: Production of Proline-Rich Proteins by the Parotid Glands of Rats Is Enhanced by Feeding Diets Containing Tannins from Faba Beans (Vicia faba L.)1'2.
This insightful overview by one of the most respected names in protein research discusses a broad array of the aspects involved with protein purification, including historical background, determining the purpose for purifying a particular protein, and actual methods and recommendations for purification Cited by: 7.
Three basic proline-rich salivary proteins have been produced through the recombinant route. IB5 is a small basic proline-rich protein that is involved in the binding of plant tannins in the oral cavity. II-1 is a larger protein with a closely related backbone; it is glycosylated, and it is also able to bind plant tannins.
II-1ng has the same polypeptidic backbone as II-1, but it is not Cited by: Parotid α-amilase activity: A possible role for proline-rich proteins FEBS LettersAnalysis of the structural forms of α-amylase present in chicken.
Proline-rich proteins (PRPs) is a class of intrinsically unstructured proteins (IUP) containing several repeats of a short proline-rich sequence. Many tannin-consuming animals secrete a tannin-binding protein in their -binding capacity of salivary mucin is directly related to its proline content.
Advantages in using salivary proline-rich proteins (PRPs) to inactivate tannins are. The parotid saliva components in lanes 3 to 7 and 10 clearly bound to fimbriae (Fig. 1B); the protein bands c and e shown in Fig. 1were PRP1 and statherin, whereas the broad bands a and b were novel fimbria-binding proteins.
The latter two bands belonged to PRGs as judged by the relative mobility and pink-violet coloration with CBB RCited by: Basic salivary proline-rich protein 1 Add BLAST: Chain i PRO_ 17 – Proline-rich peptide II-2 Add BLAST: Chain i PRO_ – Basic peptide IB-6 Add BLAST: Chain i PRO_ – Peptide P-H Add BLAST: